Specificity / Sensitivity

Cleaved Caspase Substrate Motif [DE(T/S/A)D] Rabbit mAb recognizes endogenous levels of caspase-cleaved proteins with a carboxy-terminal aspartic acid residue, and in rare cases a carboxy-terminal glutamic acid residue . This antibody does not cross-react with whole proteins or those ending with a different carboxy-terminal residue.

Source / Purification

Monoclonal antibody is produced by immunizing animals with a synthetic peptide library containing a carboxy-terminal Asp motif. The antibody is multiclonal, containing four clones to elicit broad reactivity.

Background

Apoptosis is a physiological process resulting in a highly regulated, programmed form of cell death that is a normal part of growth and development in multicellular organisms. Caspases are aspartic acid-directed cysteine proteases that are central to the apoptotic mechanism (1). The intrinsic pathway initiates an apoptotic cascade from signals originating within the cell, such as DNA damage, while an extrinsic pathway initiates apoptosis in response to extracellular signals, like FasL. In both intrinsic and extrinsic pathways, initiator caspases cleave downstream substrates, including multiple effector caspases and the primary executioner of cell death, caspase-3 (2,3). Effector caspases amplify the apoptotic cascade to target many critical proteins needed for normal cell function. Apart from its role in developmental biology, the regulation of apoptosis has broad implications for the study of cancer, autoimmune disorders and infectious diseases (4). Thousands of known and putative caspase cleavage sites are present within the human proteome; almost all sites involve cleavage at an aspartic acid residue, though cleavage at glutamic acid residues is seen, rarely, as well (5).